ID D7V0R2_LISGR Unreviewed; 451 AA.
AC D7V0R2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:EFI83144.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:EFI83144.1};
GN Name=gor {ECO:0000313|EMBL:EFI83144.1};
GN ORFNames=HMPREF0556_11829 {ECO:0000313|EMBL:EFI83144.1};
OS Listeria grayi DSM 20601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI83144.1, ECO:0000313|Proteomes:UP000010119};
RN [1] {ECO:0000313|EMBL:EFI83144.1, ECO:0000313|Proteomes:UP000010119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI83144.1,
RC ECO:0000313|Proteomes:UP000010119};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFI83144.1}.
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DR EMBL; ACCR02000005; EFI83144.1; -; Genomic_DNA.
DR RefSeq; WP_003754872.1; NZ_GL538352.1.
DR AlphaFoldDB; D7V0R2; -.
DR STRING; 525367.HMPREF0556_11829; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_2_9; -.
DR Proteomes; UP000010119; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006322; Glutathione_Rdtase_euk/bac.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01421; gluta_reduc_1; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000010119}.
FT DOMAIN 8..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 340..450
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 175..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 451 AA; 49850 MW; EB6FAA723B427B3D CRC64;
MEHVYDYDYI SIGGGSGGIA SINRAAMHGA KCALIEPNYL GGTCVNVGCV PKKVTWYGAQ
INESLNKYAA DYGIEASHKI SFEKLVANRD AYIERIRGSY KNGLDSNSVE WIKGYASFID
AHTIEVDGKQ ITAEHILIAT GGQPIYPEIK GSQYGQTSDD FFDWKTLPDR VAIVGAGYIA
VELAGLLESF EVETHLFVRK EQPLRKFDAL LSETLTEIMD KSALHLHKQA VPKEVVKNED
GSLTLYLENG ESQTVDALIW AIGRKPHFDK LALDKAGVRL TDKGYIQVDK YQNTTTEHIY
AVGDVTGKFE LTPVAIAAGR RLSERLFNGK LDEHLEYENI PTVVFSHPAI GTVGLTEAEA
IQKYGEEDIQ VYQSSFTSMY TAITENREPC KMKLICQGEN KRIVGLHGIG YGVDEMIQGF
AVAINMGATK QDFDRTVAIH PTGAEEFVTM R
//